14 research outputs found
Proteins in solution: Fractal surfaces in solutions
The concept of the surface of a protein in solution, as well of the interface
between protein and 'bulk solution', is introduced. The experimental technique
of small angle X-ray and neutron scattering is introduced and described
briefly. Molecular dynamics simulation, as an appropriate computational tool
for studying the hydration shell of proteins, is also discussed. The concept of
protein surfaces with fractal dimensions is elaborated. We finish by exposing
an experimental (using small angle X-ray scattering) and a computer simulation
case study, which are meant as demonstrations of the possibilities we have at
hand for investigating the delicate interfaces that connect (and divide)
protein molecules and the neighboring electrolyte solution.Comment: 8 pages, 5 figure
Self-Assembly of “S-Bilayers”, a Step Toward Expanding the Dimensionality of S‑Layer Assemblies
Protein-based assemblies with ordered nanometer-scale features in three dimensions are of interest as functional nanomaterials but are difficult to generate. Here we report that a truncated S-layer protein assembles into stable bilayers, which we characterized using cryogenic-electron microscopy, tomography, and X-ray spectroscopy. We find that emergence of this supermolecular architecture is the outcome of hierarchical processes; the proteins condense in solution to form 2-D crystals, which then stack parallel to one another to create isotropic bilayered assemblies. Within this bilayered structure, registry between lattices in two layers was disclosed, whereas the intrinsic symmetry in each layer was altered. Comparison of these data to images of wild-type SbpA layers on intact cells gave insight into the interactions responsible for bilayer formation. These results establish a platform for engineering S-layer assemblies with 3-D architecture
Self-Assembly of “S-Bilayers”, a Step Toward Expanding the Dimensionality of S‑Layer Assemblies
Protein-based assemblies with ordered nanometer-scale features in three dimensions are of interest as functional nanomaterials but are difficult to generate. Here we report that a truncated S-layer protein assembles into stable bilayers, which we characterized using cryogenic-electron microscopy, tomography, and X-ray spectroscopy. We find that emergence of this supermolecular architecture is the outcome of hierarchical processes; the proteins condense in solution to form 2-D crystals, which then stack parallel to one another to create isotropic bilayered assemblies. Within this bilayered structure, registry between lattices in two layers was disclosed, whereas the intrinsic symmetry in each layer was altered. Comparison of these data to images of wild-type SbpA layers on intact cells gave insight into the interactions responsible for bilayer formation. These results establish a platform for engineering S-layer assemblies with 3-D architecture